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10.1074/jbc.M808752200 http://scihub22266oqcxt.onion/10.1074/jbc.M808752200 C2685660!2685660 !19329436     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19329436 &cmd=llinks): Failed to open stream: HTTP request failed! 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Regulation of the epithelial Mg2+ channel TRPM6 by estrogen and the associated repressor protein of estrogen receptor activity (REA) |pdf=|usr=}}{{19329436 }} gab.com Text Regulation of the epithelial Mg2+ channel TRPM6 by estrogen and the associated repressor protein of estrogen receptor activity (REA) JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=19329436 #FOAvip The maintenance of the Mg(2+) balance of the body is essential for neuromuscular excitability, protein synthesis, nucleic acid stability, and numerous enzymatic systems. The Transient Receptor Potential Melastatin 6 (TRPM6) functions as the gatekeeper of transepithelial Mg(2+) transport. However, the molecular regulation of TRPM6 channel activity remains elusive. Here, we identified the repressor of estrogen receptor activity (REA) as an interacting protein of TRPM6 that binds to the 6(th), 7(th), and 8(th) beta-sheets in its alpha-kinase domain. Importantly, REA and TRPM6 are coexpressed in renal Mg(2+)-transporting distal convoluted tubules (DCT). We demonstrated that REA significantly inhibits TRPM6, but not its closest homologue TRPM7, channel activity. This inhibition occurs in a phosphorylation-dependent manner, since REA has no effect on the TRPM6 phosphotransferase-deficient mutant (K1804R), while it still binds to this mutant. Moreover, activation of protein kinase C by phorbol 12-myristate 13-acetate-PMA potentiated the inhibitory effect of REA on TRPM6 channel activity. Finally, we showed that the interaction between REA and TRPM6 is a dynamic process, as short-term 17beta-estradiol treatment disassociates the binding between these proteins. In agreement with this, 17beta-estradiol treatment significantly stimulates the TRPM6-mediated current in HEK293 cells. These results suggest a rapid pathway for the effect of estrogen on Mg(2+) homeostasis in addition to its transcriptional effect. Together, these data indicate that REA operates as a negative feedback modulator of TRPM6 in the regulation of active Mg(2+) (re)absorption and provides new insight into the molecular mechanism of renal transepithelial Mg(2+) transport. Twit Text FOAVip Regulation of the epithelial Mg2+ channel TRPM6 by estrogen and the associated repressor protein of estrogen receptor activity (REA) ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=19329436 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19329436 #FOAvip English Wikipedia <ref>{{Cite pmid|19329436 }}</ref> Regulation of the epithelial Mg2+ channel TRPM6 by estrogen and the associated repressor protein of estrogen receptor activity (REA) #MMPMID19329436 Cao G ; van der Wijst J ; van der Kemp A ; van Zeeland F ; Bindels RJ ; Hoenderop JG J Biol Chem 2009[May]; 284 (22 ): 14788-95 PMID19329436 show ga The maintenance of the Mg(2+) balance of the body is essential for neuromuscular excitability, protein synthesis, nucleic acid stability, and numerous enzymatic systems. The Transient Receptor Potential Melastatin 6 (TRPM6) functions as the gatekeeper of transepithelial Mg(2+) transport. However, the molecular regulation of TRPM6 channel activity remains elusive. Here, we identified the repressor of estrogen receptor activity (REA) as an interacting protein of TRPM6 that binds to the 6(th), 7(th), and 8(th) beta-sheets in its alpha-kinase domain. Importantly, REA and TRPM6 are coexpressed in renal Mg(2+)-transporting distal convoluted tubules (DCT). We demonstrated that REA significantly inhibits TRPM6, but not its closest homologue TRPM7, channel activity. This inhibition occurs in a phosphorylation-dependent manner, since REA has no effect on the TRPM6 phosphotransferase-deficient mutant (K1804R), while it still binds to this mutant. Moreover, activation of protein kinase C by phorbol 12-myristate 13-acetate-PMA potentiated the inhibitory effect of REA on TRPM6 channel activity. Finally, we showed that the interaction between REA and TRPM6 is a dynamic process, as short-term 17beta-estradiol treatment disassociates the binding between these proteins. In agreement with this, 17beta-estradiol treatment significantly stimulates the TRPM6-mediated current in HEK293 cells. These results suggest a rapid pathway for the effect of estrogen on Mg(2+) homeostasis in addition to its transcriptional effect. Together, these data indicate that REA operates as a negative feedback modulator of TRPM6 in the regulation of active Mg(2+) (re)absorption and provides new insight into the molecular mechanism of renal transepithelial Mg(2+) transport. |Animals [MESH] |Cell Line [MESH] |Epithelial Cells/*drug effects/*metabolism [MESH] |Estradiol/*pharmacology [MESH] |Gene Expression Profiling [MESH] |Humans [MESH] |Ion Channel Gating/drug effects [MESH] |Kidney/metabolism [MESH] |Mice [MESH] |Phosphorylation/drug effects [MESH] |Prohibitins [MESH] |Protein Binding/drug effects [MESH] |Protein Structure, Secondary [MESH] |Protein Structure, Tertiary [MESH] |Repressor Proteins/*metabolism [MESH]Regulation of the epithelial Mg2+ channel TRPM6 by estrogen and the as(epmc).pdf DeepDyve Pubget Overpricing